Caenorhabditis elegans is a transparent roundworm that functions as an ideal model organism for studying the complex processes that occur during embryonic cell division. The cell division process is comprised of distinct phases that ensure the development of a healthy and robust embryo. The cytokinesis phase is characterized by the formation of a contractile ring near the middle of the embryo. When this contractile ring constricts, the embryo can effectively divide into two cells. Recent work in the Lyczak laboratory has focused on better understanding how the aminopeptidase PAM-1 works in conjunction with cytoskeletal proteins to regulate the actomyosin cytoskeleton. PAM-1 is localized throughout the entire cytoplasm in developing C. elegans embryos. Anillin (ANI-1), non-muscle myosin (NMY-2), and ezrin/radixin/moesin (ERM-1) are three cytoskeletal proteins that are necessary for appropriate cytoskeleton contractility. SPD-1 is a different cytoskeletal protein that is required for the development of the spindle midzone, which is a key component that forms when the contractile ring constricts. This semester, I prepared a research proposal to explore the relationship between SPD-1 and PAM-1. The goal of this proposal is to use a variety of microscopy techniques to clarify any interactions between these 3 cytoskeletal contractility proteins, SPD-1, and PAM-1.
Ayala, Alexis, "Research Proposal: Clarifying Any Interactions Between Cytoskeletal Proteins and the Aminopeptidase PAM-1" (2021). Biology Presentations. 28.
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